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From recognition to execution-the HCMV Pentamer from receptor binding to fusion triggering
Enrico Malito1, Sumana Chandramouli1, Andrea Carfi2
1GSK, 14200 Shady Grove Road, Rockville, MD 20850, USA.
Current Opinion in Virology
|June 6, 2018
Summary
Human cytomegalovirus (HCMV) uses its pentameric glycoprotein complex to bind cell receptors, triggering membrane fusion. This process is crucial for HCMV infection and understanding its role in neonatal disabilities.
Area of Science:
- Virology
- Molecular Biology
- Immunology
Background:
- Human cytomegalovirus (HCMV) is a major cause of congenital disabilities.
- HCMV entry relies on glycoprotein B (gB) for membrane fusion and the pentameric complex (Pentamer) for receptor binding and signaling.
Purpose of the Study:
- To elucidate the structural and functional mechanisms of the HCMV Pentamer complex.
- To understand how receptor binding by the Pentamer complex initiates viral entry.
Main Methods:
- Structural biology techniques (e.g., cryo-EM, X-ray crystallography).
- Biochemical assays to study protein-protein interactions.
- Functional assays to assess viral entry and fusion.
Main Results:
- Detailed structural insights into the Pentamer complex, revealing its conformational flexibility.
- Identification of key epitopes for neutralizing antibodies.
- Mapping potential cell surface receptor binding sites on the Pentamer.
Conclusions:
- Receptor binding induces a conformational change in the Pentamer complex.
- This conformational change enables interaction with gB, initiating viral-host membrane fusion.
- Findings provide a model for HCMV entry and targets for antiviral therapies.
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